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Physics Prize: Weiss, Barish, and Thorne’s gravitational waves

Over a billion years ago, two black holes collided. After a long, drawn-out approach in which they gradually orbited each other more and more closely, the two gargantuan bodies crashed. The impact sent ripples through the universe at the speed of light, stretching and squashing spacetime itself as they passed.

Two years ago, on 14 September 2015, these momentary deformations passed through two detectors in Washington and Louisiana, USA.

In keeping with Einstein’s century-old theory of General Relativity, these ripples, known as gravitational waves, shortened spacetime in one direction and elongated it in another, much like when a block of rubber is squeezed. Unlike a block of rubber, however, it was not solely the material that was deformed, but space itself and everything in it.

So, as lasers were fired down two arms of the L-shaped detectors, one beam had to travel slightly more distance, and the other slightly less. This tiny discrepancy between the returning beams became one of the most important pieces of evidence for Einstein’s theory.

The signals picked up by the detectors were analysed by a collaboration between two institutions, Virgo and Laser Interferometer Gravitational-Wave Observatory (LIGO).

Out of a thousand scientists, engineers, and mathematicians, only three could be chosen to win the Nobel Prize.

After lengthy discussion with experts in the field, Rainer Weiss, Barry C Barish and Kip S Thorne were selected to receive the prize.

They were described as ‘key figures’ in the project’s success: “They represent well the diverse competencies needed for LIGO’s success: from detector design and understanding of sources to integration and evolution.”

“All three were indispensable”, said Olga Botner, member of the Nobel Committee for Physics.

This is only the beginning of the discoveries to be made regarding gravitational waves.

The phenomenon will provide an exciting new way to probe the darkest corners and furthest reaches of the universe.

–Sara Rigby

Medicine Prize: Hall, Rosbash, Young and circadian rhythm

Early Monday morning, the Nobel Prize awarding institution called Jeffrey C Hall, Michael Rosbash and Michael W Young to let them know that they’d been awarded the 2017 Nobel prize in Physiology or Medicine “for their discoveries of mechanisms controlling circadian rhythms.”

For Rosbash, the call from Stockholm was a bit ironic, seeing that it woke him up around 5:00 a.m. California time and disrupted his own sleep cycle.

Research into the genetics of circadian rhythms has been of high interest in recent years due to the accumulation of evidence suggesting that the biological clock in humans affects not only sleeping patterns, but also productivity, metabolism, mood swings and risk levels for disease.

By working with the genetics of the biological clock, the research by Hall, Rosbash and Young has promoted the value of having healthy sleeping habits in an increasingly nocturnal world.

Rosbash must be no stranger to the effects of sleep deprivation, not only because it is tied to his research, but also because he spent three years at the University of Edinburgh in the 1970s working on his postdoctoral fellowship in genetics. He has been working at Brandeis University in California ever since.

Young, a professor at Rockefeller University in New York, was drawn to the field at a young age when he noticed a houseplant which consistently opened and closed its flowers depending on the time of day. He has since been credited with the discovery of two genes responsible for regulating circadian rhythms. Hall retired over a decade ago and currently lives in Maine. Rumours that he left academia due to frustrations with corruption and a lack of funding have been earning Hall more media attention in light of the recent award, which he said was largely unexpected.

–Julia Haines

Chemistry Prize: Dubochet, Frank and Henderson’s microscopy

This year the chemistry prize goes jointly to Jacques Dubochet of the University of Lausanne in Switzerland, Joachim Frank of Columbia University, and Richard Henderson of the Medical Research Council Laboratory of Molecular Biology (LMB) in Cambridge, UK. Together, they have pioneered a technique called ‘cryoelectron microscopy’, which can deduce high resolution images of protein structure, right down to the level of individual atoms.

The accolade is recognition for work done largely in the 70s and 80s, which “moved biochemistry into a new era”, according to the Royal Swedish Academy of Sciences, who award the Nobel prize.

Dr Henderson proved the potential of the technique. In the 1970s, he was trying to determine the shape of a protein called bacteriorhodopsin, which uses energy from light to move protons across a cell membrane.

Although he tried, he could not get the proteins in the membrane to crystallise for imaging. Instead, he turned to electron microscopy (EM). Using diffraction patterns and the orderly arrangement of molecules in the membrane, he became the first to create a 3D image of a protein using EM.

Dr Frank and colleagues developed image processing software that can deduce the 3D structure of a protein from the fuzzy, flat images produced by an electron microscope. His algorithms made Henderson’s technique functional for proteins that don’t occur in such an organised way, and thus massively increased the reach of the technology.

Dr Dubochet invented a method of ‘flash-freezing’ solutions of proteins. When biological samples are frozen in water, the ice crystals diffract light and blur the image. But speed is key: Dubochet found that if water is frozen quick enough, instead of crystallising, it becomes glass-like, and can keep molecules still while they are being imaged. This allows researchers to see proteins in various stages of movement, and compile photos to create a film that recreates their action inside cells.

His technique allowed Henderson to create the first atomic image of a protein using cryoelectron microscopy in 1990.

Using cryoelectron microscopy, researchers can visualise processes they have never seen before; this has been an enormous boon in pharmaceutical development (where knowledge of protein shape can help to direct drug design) and for understanding human biochemistry.

It hasn’t always been plain-sailing for the scientists: Dubochet’s method was once dubbed ‘blobology’ because of the low resolution first images it produced. However, in coordinating their work, the scientists have enabled a much clearer view of the microscopic world. Undoubtedly, a deserved win.